Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.febslet.2009.02.022
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dc.titleInsight into "insoluble proteins" with pure water
dc.contributor.authorSong, J.
dc.date.accessioned2011-11-29T05:58:36Z
dc.date.available2011-11-29T05:58:36Z
dc.date.issued2009
dc.identifier.citationSong, J. (2009). Insight into "insoluble proteins" with pure water. FEBS Letters 583 (6) : 953-959. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2009.02.022
dc.identifier.issn00145793
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/28714
dc.description.abstractMany proteins are not refoldable and also insoluble. Previously no general method was available to solubilize them and consequently their structural properties remained unknown. Surprisingly, we recently discovered that all insoluble proteins in our laboratory, which are highly diverse, can be solubilized in pure water. Structural characterization by CD and NMR led to their classification into three groups, all of which appear trapped in the highly disordered or partially-folded states with a substantial exposure of hydrophobic side chains. In this review, I discuss our results in a wide context and subsequently propose a model to rationalize the discovery. The potential applications are also explored in studying protein folding, design and membrane proteins. © 2009 Federation of European Biochemical Societies.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.febslet.2009.02.022
dc.sourceScopus
dc.subjectCircular dichroism (CD)
dc.subjectInsoluble protein
dc.subjectIonic strength
dc.subjectNMR
dc.subjectProtein folding
dc.subjectProtein solubility
dc.subjectWater
dc.typeOthers
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/j.febslet.2009.02.022
dc.description.sourcetitleFEBS Letters
dc.description.volume583
dc.description.issue6
dc.description.page953-959
dc.description.codenFEBLA
dc.identifier.isiut000264761500001
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